Ex Parte Tryggvason et al

Patent Trial and Appeal Board

Jun 10, 2016

13409594 (P.T.A.B. Jun. 10, 2016)

UNITED STATES PATENT AND TRADEMARK OFFICE
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O. Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
13/409,594 03/01/2012 Karl Tryggvason LCTI 200005US01 1082
27885 7590 06/10/2016
FAY SHARPE LLP
1228 Euclid Avenue, 5th Floor
The Halle Building
Cleveland, OH 44115
EXAMINER
HELLMAN, KRISTINA M
ART UNIT PAPER NUMBER
1675
MAIL DATE DELIVERY MODE
06/10/2016 PAPER
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
PTOL-90A (Rev. 04/07)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte KARL TRYGGVASON and SERGEY RODIN

____________

Appeal 2014-005063
Application 13/409,5941
Technology Center 1600
____________

Before DONALD E. ADAMS, RICHARD M. LEBOVITZ, and
ULRIKE W. JENKS, Administrative Patent Judges.

LEBOVITZ, Administrative Patent Judge.

DECISION ON APPEAL
This appeal involves claims directed to isolated recombinant laminin-
421. Appellants appeal from the Examiner’s final rejection of claims 1–5
and 9–14 as lacking a written description under 35 U.S.C. § 112. We have
jurisdiction under 35 U.S.C. § 134. The rejection is affirmed. We also enter
a new grounds of rejection of claims 6 and 7 as lacking a written description
under 35 U.S.C. § 112.

1 The application disclosure is referred to herein as the “Specification.”
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Application 13/409,594

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STATEMENT OF CASE
Claims 1–5 and 9–14 stand finally rejected by the Examiner as failing
to comply with the written description requirement under 35 U.S.C. § 112,
first paragraph (pre-AIA). Final Rej. 2.

Claims
Claim 1 is a product-by-process claim drawn to recombinant laminin-
421 isolated by a specific method. Claim 2 is drawn to isolated recombinant
laminin-421. Appellants did not argue the claims separately. Accordingly,
they stand or fall together. 37 C.F.R. § 41.37(c)(iv). We select claim 2 as
representative of the claimed subject matter. Claim 2 reads as follows:
2. An isolated recombinant laminin-421, comprising:
a first chain comprising a polypeptide with at least 80%
identity to a polypeptide sequence of SEQ ID NO: 1;
a second chain comprising a polypeptide with at least
70% identity to a polypeptide sequence of SEQ ID NO: 2; and
a third chain comprising a polypeptide with at least 70%
identity to a polypeptide sequence of SEQ ID NO: 3;
wherein the first, second, and third chains are assembled
into recombinant laminin-421.

Claim 2 is directed to an isolated recombinant laminin-421 which
comprises three polypeptide chains. The first chain comprises a polypeptide
with at least 80% identity to a polypeptide sequence of SEQ ID NO: 1. The
second chain comprises a polypeptide with at least 70% identity to a
polypeptide sequence of SEQ ID NO: 2. The third chain comprises a
polypeptide with at least 70% identity to a polypeptide sequence of SEQ ID
NO: 3. The first, second, and third chains “are assembled into recombinant
laminin-421.”
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Rejection
The Examiner rejected the claims as lacking a written description
under 35 U.S.C. § 112. The Examiner found that the claims encompass
80%, 70%, and 70% identity to SEQ ID NOS. 1, 2, and 3, respectively, but
the Specification only discloses one example of a laminin-421 with 100%
identity to the recited SEQ ID NOS. Final Rej. 4–5. The Examiner found
that the claims recited a genus of polypeptides represented by the recited
sequence identity. Id. Citing MPEP § 2163, the Examiner stated that a
representative number of species is necessary to support the claimed genus
of polypeptides. Id. at 5. The Examiner found that the Specification only
disclosed one species of laminin-421 and did not describe the minimal
amino acid sequence of SEQ ID NOS. 1, 2, and 3 necessary to maintain the
functional activity of laminin-421. Id. Because the Specification did not
describe a correlation between the structure and function of each of three
laminin chains and laminin-421, the Examiner concluded that the claims
were not in compliance with the written description requirement of 35
U.S.C. § 112. Id. at 6–7.

Discussion
35 U.S.C. § 112 requires a patentee to provide a written description of
the claimed subject matter that allows a person of skill in the art to recognize
that the patentee invented what is claimed. Ariad Pharms., Inc. v. Eli Lilly
& Co., 598 F.3d 1336, 1351 (Fed. Cir. 2010) (en banc). In University of
California v. Eli Lilly & Co. (“Lilly”), 119 F.3d 1559 (Fed. Cir. 1997), the
Federal Circuit set forth a test for compliance with the written description
requirement when a genus of recombinant sequences is claimed. In Lilly,
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only a single cDNA to rat insulin was described in the patent specification,
but the Patentee had claims that covered broader genera of cDNAs, coding
for mammalian and vertebrate insulins, respectively. Lilly, 119 F.3d at
1563, 1567. In an infringement suit, the validity of these claims was
challenged. The Lilly court held the claims invalid for failing to provide an
adequate written description of the claimed genus. The court wrote:
In claims to genetic material, however, a generic statement such
as “vertebrate insulin cDNA” or “mammalian insulin cDNA,”
without more, is not an adequate written description of the
genus because it does not distinguish the claimed genus from
others, except by function. It does not specifically define any
of the genes that fall within its definition. It does not define
any structural features commonly possessed by members of the
genus that distinguish them from others. One skilled in the art
therefore cannot, as one can do with a fully described genus,
visualize or recognize the identity of the members of the genus.
Id. at 119 F.3d at 1568.
Consistent with Lilly, it was held in Enzo Biochem, Inc. v. Gen-Probe
Inc., 323 F.3d 956, 964 (Fed. Cir. 2002):
[T]he written description requirement can be met by “show[ing]
that an invention is complete by disclosure of sufficiently
detailed, relevant identifying characteristics . . . i.e., complete or
partial structure, other physical and/or chemical properties,
functional characteristics when coupled with a known or
disclosed correlation between function and structure, or some
combination of such characteristics.”
In sum, to meet the written description requirement, the Specification
must describe “structural features commonly possessed by members of the
genus that distinguish them from others” (Lilly, 119 F.3d at 1568), such as
“a known or disclosed correlation between function and structure.” Enzo
Biochem, 323 F.3d at 964.
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Appellants contend that the Specification provided a “disclosure
regarding the correlation between structure and function.” Appeal Br. 8. To
support this statement, Appellants identify the following disclosure in the
Specification: “paragraphs [0057] (discussion of folding characteristics),
[0012] (discussion of different binding domains / cysteine rich EGF-like
domains), and [0003]-[0010] (discussion of the role and function of basal
lamina).” Id. Before we review the referenced disclosures, we shall address
the functional requirements of the claims.
Each of independent claims 1 and 2, require the three chains to have
assembled into recombinant laminin-421. Consequently, the claim at
minimum requires that each chain have the functional ability to assemble
with the other two chains to form a laminin-421. In addition, laminin-421 is
described in the Specification as being for “cell attachment.” Spec. ¶¶ 21,
73. However, the subsequent definition of laminin-421 at paragraph 37 of
the Specification does not enumerate its functions. Consequently, it is not
clear whether the recitation of “laminin-421” requires it to be a completely
functional molecule. Thus, for the purpose of our analysis, we will focus on
the function of all three chains to assemble into a laminin-421 molecule
because that is an express requirement of the claim.
Appellants referenced paragraphs 3–10 of the Specification in support
of the written description for the claims. Appeal Br. 8. These paragraphs
described the role of the basal lamina present in “virtually all tissues.” Spec.
¶ 3. Paragraph 9 teaches that basal lamina contains laminin. Paragraph 10
describes functions of laminin, such as “binding to other laminin molecules
or other matrix proteins such as collagens, nidogens or proteoglycans” and
“maintaining cell/tissue phenotype as well as promoting cell growth and
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differentiation in tissue repair and development.” We do not find a
description of a structural feature of laminin-421 in the referenced
paragraphs 3–10 that are responsible for the recited functions, let alone for
the ability of all three chains to assemble together.
Paragraph 12 of the Specification, also identified by Appellants for
written description support, teaches that a “laminin molecule is comprised of
one α-chain subunit, one β-chain subunit, and one γ-chain subunit, all joined
together through a coiled-coil domain.” This activity appears to be pertinent
to the claimed requirement that the three chains assemble together to form
laminin-421. However, the Specification does not disclose the location of
the coil-coil domain nor the structural features of it which would be
necessary to join the subunit chains together.
It is also disclosed in paragraph 12 that “Domains I and II of the three
chains participate in the formation of a triple-stranded coiled-coil.” Once
again, there is no description of the structure of these domains nor the
necessary structural requirements for Domains I and II to participate in the
formation of the coiled-coil. Thus, while paragraph 12 appears to identify
structures involved in assembly, e.g., coiled-coil domain, Domain I, and
Domain II, there is no description of the specific amino acid structure of
these domains, their location in the polypeptide chains, nor what amino acids
could be changed to achieve the recited percent identity and still possess the
required activity in joining or assembling the chains together. Consequently,
we do not find this disclosure adequate to support the written description of
the full scope of the claim.
In paragraph 57 referred to by Appellants, expression of recombinant
laminin-421 is described. It is stated that “[c]arbohydrate and disulfide
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posttranslational modifications are believed to be required for laminin-421
protein folding and function.” While such modifications may be necessary
for function, paragraph 57 does not identify where these modifications are
made to the three laminin-421 chains. We therefore find this disclosure
insufficient because it does not specifically identify a structural feature of
the genus necessary to retain assembly activity and which distinguishes it
from other proteins.
Appellants argue that the Specification identifies domains of the
claimed polypeptide chains and that one of ordinary skill in the art would
expect that conservative amino acid mutations in the domains would result
in a protein having the required activity. Appeal Br. 10–11. This argument
is not persuasive. The Specification discloses that a coiled-coil domain is
involved in joining the laminin chains together, but has not provided any
information on what parts of the α, β, and γ chain are involved in making
such domain. Therefore, Appellants have not established a correlation
between the structure of the chains and their function to assemble together.
The disclosure that the polypeptides join through a coiled-coil domain and
have Domains I and II is not “sufficiently detailed” to allow the skilled
worker to visualize the members of the genus (Enzo, 323 F.3d at 964)
because it doesn’t provide the location or structure of the domain in the
recited chains and laminin-421. In our opinion, a written description of a
genus of polypeptides is more than just a recitation of domains found in the
genus, but requires a more detailed picture of the genus, e.g., identifying the
location of the domains in the genus of polypeptides and their amino acid
sequence.
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Appellants contend that “knowledge” of what amino acids could be
varied and still maintain the functionality of a laminin protein “is within the
ordinary skill of the art” (id. at 12), but did not provide evidence to support
this position.
In sum, we find that the Examiner met the initial burden in presenting
by evidence why a person skilled in the art would not recognize in the
disclosure a description of the invention defined by the claims. In re
Wertheim, 541 F.2d 257, 263 (CCPA 1976). Appellants did not provide
adequate evidence to establish an error in the Examiner’s determination.
Consequently, we affirm the rejection of claims 1 and 2. Claims 3–5 and 9–
14 fall with claims 1 and 2.

NEW GROUND OF REJECTION
Claim 6 depends from claim 2, and recites that the first chain has the
polypeptide sequence of SEQ ID NO: 1. The second and third chains have
the recited percent identity of claim 2, i.e., 70% and 70%, respectively.
Claim 7 depends from claim 6, and recites that the second chain has
the polypeptide sequence of SEQ ID NO: 2. The third chain has the recited
percent identity of claim 2, i.e., 70%.
Both claims 6 and 7 have the same deficiency identified for claims 1
and 2, namely reciting a genus of polypeptide chains with sequence identity
to a sequence identifier, but not describing the genus of polypeptides in the
Specification in accordance with Lilly. With claim 2, all three chains have a
percent identity. With claim 6, it’s two chains, and one chain with claim 7.
However, each have the same defect as claim 2, namely, reciting a genus of
polypeptides but no written description support for the genus. The Examiner
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did not provide an explanation as to why claims 6 and 7, which are drawn to
a genus of polypeptides, are described by the Specification, while claim 2 is
not. Accordingly, we are set forth a new ground of rejection of claims 6 and
7 as failing to comply with the written description requirement of 35 U.S.C.
§ 112, first paragraph.

TIME PERIOD
Regarding the affirmed rejection(s), 37 C.F.R. § 41.52(a)(1) provides
“Appellant may file a single request for rehearing within two months from
the date of the original decision of the Board.”
In addition to affirming the Examiner’s rejection(s) of one or more
claims, this decision contains a new ground of rejection pursuant to 37
C.F.R. § 41.50(b). 37 C.F.R. § 41.50(b) provides “[a] new ground of
rejection pursuant to this paragraph shall not be considered final for judicial
review.”
37 C.F.R. § 41.50(b) also provides that the Appellant, WITHIN TWO
MONTHS FROM THE DATE OF THE DECISION, must exercise one of
the following two options with respect to the new ground of rejection to
avoid termination of the appeal as to the rejected claims:
(1) Reopen prosecution. Submit an appropriate amendment of
the claims so rejected or new evidence relating to the claims so
rejected, or both, and have the matter reconsidered by the
examiner, in which event the proceeding will be remanded to
the examiner….

(2) Request rehearing. Request that the proceeding be reheard
under § 41.52 by the Board upon the same record….

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Should the Appellant elect to prosecute further before the Examiner
pursuant to 37 C.F.R. § 41.50(b)(1), in order to preserve the right to seek
review under 35 U.S.C. §§ 141 or 145 with respect to the affirmed rejection,
the effective date of the affirmance is deferred until conclusion of the
prosecution before the Examiner unless, as a mere incident to the limited
prosecution, the affirmed rejection is overcome.
If the Appellant elects prosecution before the Examiner and this does
not result in allowance of the application, abandonment or a second appeal,
this case should be returned to the Patent Trial and Appeal Board for final
action on the affirmed rejection, including any timely request for rehearing
thereof.
AFFIRMED; 41.50(b)